Evidence map›Paper›PMID 35333570›Full record

ArticleScience advances2022

Structure and dynamics of Odinarchaeota tubulin and the implications for eukaryotic microtubule evolution.

Caner Akıl, Samson Ali, Linh T Tran, Jérémie Gaillard, Wenfei Li, Kenichi Hayashida, Mika Hirose, Takayuki Kato, Atsunori Oshima, Kosuke Fujishima and 3 more

Open access · goldAbstract read
In one paragraph

Article in Science advances, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
2.6field-weighted citation impact, top 9% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

13 citing papers in PubMed, 32 citations in OpenAlex.

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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

13 authors at 6 institutions in 4 countries.

Caner AkılResearch Institute for Interdisciplinary Science, Okayama University, Okayama 700-8530, Japan.ORCID 0000-0002-9464-1903
Samson AliResearch Institute for Interdisciplinary Science, Okayama University, Okayama 700-8530, Japan.ORCID 0000-0002-1410-990X
Linh T TranResearch Institute for Interdisciplinary Science, Okayama University, Okayama 700-8530, Japan.ORCID 0000-0003-0654-6517
Jérémie GaillardUniversity of Grenoble-Alpes, CEA, CNRS, INRA, Interdisciplinary Research Institute of Grenoble, Laboratoire de Physiologie Cellulaire & Végétale, CytoMorpho Lab, 38054 Grenoble, France.ORCID 0000-0002-6943-8874
Wenfei LiNational Laboratory of Solid State Microstructure, Department of Physics, Collaborative Innovation Center of Advanced Microstructures, Nanjing University, 210093 Nanjing, China.ORCID 0000-0003-2679-4075
Kenichi HayashidaCellular and Structural Physiology Institute (CeSPI), Nagoya University, Furo-cho, Chikusa-ku, Nagoya 464-8601, Japan.
Mika HiroseInstitute for Protein Research, Osaka University, Osaka 565-0871, Japan.ORCID 0000-0001-8991-587X
Takayuki KatoInstitute for Protein Research, Osaka University, Osaka 565-0871, Japan.ORCID 0000-0002-8879-6685
Atsunori OshimaCellular and Structural Physiology Institute (CeSPI), Nagoya University, Furo-cho, Chikusa-ku, Nagoya 464-8601, Japan.ORCID 0000-0003-1174-1368
Kosuke FujishimaTokyo Institute of Technology, Earth-Life Science Institute (ELSI), Tokyo 152-8551, Japan.
Laurent BlanchoinUniversity of Grenoble-Alpes, CEA, CNRS, INRA, Interdisciplinary Research Institute of Grenoble, Laboratoire de Physiologie Cellulaire & Végétale, CytoMorpho Lab, 38054 Grenoble, France.
Akihiro NaritaDivision of Biological Science, Graduate School of Science, Nagoya University, Furo-cho, Chikusa-ku, Nagoya 464-8601, Japan.ORCID 0000-0003-1504-9352
Robert C RobinsonResearch Institute for Interdisciplinary Science, Okayama University, Okayama 700-8530, Japan.ORCID 0000-0001-6367-6903
Nagoya University · JPOkayama University of Science · JPCentre National de la Recherche Scientifique · FRProtein Research Foundation · JPTokyo Institute of Technology · JPCollaborative Innovation Center of Advanced Microstructures · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Tubulins are critical for the internal organization of eukaryotic cells, and understanding their emergence is an important question in eukaryogenesis. Asgard archaea are the closest known prokaryotic relatives to eukaryotes. Here, we elucidated the apo and nucleotide-bound x-ray structures of an Asgard tubulin from hydrothermal living Odinarchaeota (OdinTubulin). The guanosine 5'-triphosphate (GTP)-bound structure resembles a microtubule protofilament, with GTP bound between subunits, coordinating the "+" end subunit through a network of water molecules and unexpectedly by two cations. A water molecule is located suitable for GTP hydrolysis. Time course crystallography and electron microscopy revealed conformational changes on GTP hydrolysis. OdinTubulin forms tubules at high temperatures, with short curved protofilaments coiling around the tubule circumference, more similar to FtsZ, rather than running parallel to its length, as in microtubules. Thus, OdinTubulin represents an evolutionary stage intermediate between prokaryotic FtsZ and eukaryotic microtubule-forming tubulins.

Indexed as

Eukaryotic CellsTubulinEukaryotaGuanosine TriphosphateMicrotubulesGuanosine TriphosphateTubulin

Identifiers

PMID35333570
PMCPMC8956254
OpenAlexW4220897288

What OpenQuestion holds

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.